Hostname: page-component-cd9895bd7-gbm5v Total loading time: 0 Render date: 2024-12-26T00:39:31.109Z Has data issue: false hasContentIssue false
  • English
  • Français

Cysteine metabolism in the cestode Hymenolepis diminuta

Published online by Cambridge University Press:  06 April 2009

M. Gomez-Bautista  and
J. Barrett
M. Gomez-Bautista
Affiliation:
Departamento de Parasitologia, Facultad de Farmacia, Universidad de Salamanca, Salamanca, Spain
J. Barrett*
Affiliation:
Department of Zoology, University College of Wales, Aberystwyth, U.K.
*
Reprint requests to: Professor J. Barrett, Department of Zoology, University College of Wales, Aberystwyth, Dyfed SY23 3DA.
Get access Rights & Permissions [Opens in a new window]

Summary

The major pathways for cysteine catabolism in Hymenolepis diminuta have been investigated. The parasite has an active cystathionine-β-synthase and, as in other tissues, this enzyme has a wide substrate specificity. However, the enzyme from H. diminuta differs significantly from the mammalian enzyme in showing a high serine sulphydrase activity and a high serine lyase activity. There was only low γ-cystathionase activity in H. diminuta and again the enzyme showed a range of substrate specificities. Cysteine aminotransferase activity was readily demonstrated in the tapeworm, but there was no evidence for 3-mercaptopyruvate sulphotransferase activity. An oxidative pathway for cysteine catabolism in H. diminuta was shown by the presence of cysteine dioxygenase and cysteine sulphinate transaminase. The properties of the helminth cysteine dioxygenase were very similar to those of rat liver. H. diminuta was able to reduce cystine to cysteine via a glutathione-cysteine transhydrogenase system.

Type
Research Article
Information
Parasitology , Volume 97 , Issue 1 , August 1988 , pp. 149 - 159
Copyright
Copyright © Cambridge University Press 1988

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Bernt, E. & Bergmeyer, H. U. (1974). L-Glutamate UV-assay with glutamate dehydrogenase and NAD. In Methods of Enzymatic Analysis, vol. 4, 2nd ed. (ed. Bergmeyer, H. U.), pp. 1704–8. New York: Academic Press.CrossRefGoogle Scholar
Braunstein, A. E., Goryachenkova, E. V. & Lac, Nguyen Dinh (1969). Reactions catalysed by serine sulfhydrase from chicken liver. Biochimica et Biophysica Acta 171, 366–8.CrossRefGoogle ScholarPubMed
Braunstein, A. E., Goryachenkova, E. V., Tolosa, E. A., Willhardt, I. H. & Yefremova, L. L. (1971). Specificity and some other properties of liver serine sulphydrase: evidence for its identity with cystathionine synthase. Biochimica et Biophysica Acta 242, 247–60.CrossRefGoogle Scholar
Cain, G. D. & Fairbairn, D. (1971). Protocollagen proline hydroxylase and collagen synthesis in developing eggs of Ascaris lumbricoides. Comparative Biochemistry and Physiology 40B, 165–79.Google ScholarPubMed
Czok, R. & Lamprecht, W. (1974). Pyruvate, phosphoenolpyruvate and D-glycerate-2-phosphate. In Methods of Enzymatic Analysis, vol. 3, 2nd ed. (ed Bergmeyer, H. U.), pp. 1446–8. New York: Academic Press.Google Scholar
Dean, R. B. & Dixon, W. J. (1951). Simplified statistics for small numbers of observations. Analytical Chemistry 23, 636–8.CrossRefGoogle Scholar
Eriksson, S. A. & Mannervik, B. (1970). The reduction of the L-cysteine-glutathione mixed disulphide in rat liver. Involvement of an enzyme catalyzing thiol-disulphide interchange. FEBS Letters 7, 26–8.CrossRefGoogle Scholar
Ewetz, L. & Sörbo, B. (1966). Characteristics of the cysteinesulfinate-forming enzyme system in rat liver. Biochimica et Biophysica Acta 128, 296–305.CrossRefGoogle ScholarPubMed
Grant, W. M. (1947). Colorimetric determination of sulfur dioxide. Analytical Chemistry 19, 345–6.CrossRefGoogle Scholar
Greenberg, D. M. (1975). Metabolic Pathways: Sulphur Compounds, vol. 7, 3rd ed. New York: Academic Press.Google Scholar
Kashiwamata, S. & Greenberg, D. M. (1970). Studies on cystathionine synthase of rat liver properties of the highly purified enzyme. Biochimica et Biophysia Acta 212, 488–500.CrossRefGoogle ScholarPubMed
Leinweber, F. -J. & Monty, K. J. (1962). Microdetermination of cysteine sulfinic acid. Analytical Biochemistry 4, 252–6.CrossRefGoogle Scholar
Lombardini, J. B., Turini, P., Biggs, D. R. & Singer, T. P. (1969). Cysteine oxygenase. 1. General properties. Physiological Chemistry and Physics 1, 1–23.Google Scholar
Mudd, H. S., Finkelstein, J. D., Irreverre, F. & Laster, L. (1965). Transsulfuration in mammals, microassays and tissue distributions of three enzymes of the pathway. Journal of Biological Chemistry 240, 4382–92.CrossRefGoogle ScholarPubMed
Munir, W. A. & Barrett, J. (1985). The metabolism of xenobiotic compounds by Hymenolepis diminuta (Cestoda: Cyclophyllidea). Parasitology 91, 145–56.CrossRefGoogle Scholar
Mushahwar, I. K. & Koeppe, R. E. (1973). Rat liver diaminopropionate ammonia lyase, identification as cystathionase. Journal of Biological Chemistry 248, 7407–11.CrossRefGoogle ScholarPubMed
Pieniazek, N. J., Stepien, P. P. & Paszewski, A. (1973). An Aspergillus nidulans mutant lacking cystathionine-β-synthase: identity of L-serine sulfhydrylase with cystathionine-β-synthase and its distinctness from O-acetyl-L-serine sulfhydrylase. Biochimica et Biophysica Acta 297, 37–47.CrossRefGoogle Scholar
Ribeiro, P. & Webb, R. A. (1983 a). The occurrence and synthesis of octopamine and the catechol amines in the cestode Hymenolepis diminuta. Molecular and Biochemical Parasitology 7, 53–62.CrossRefGoogle ScholarPubMed
Ribeiro, P. & Webb, R. A. (1983 b). The synthesis of 5-hydroxytryptamine from tryptophan and 5-hydroxytryptophan in the cestode Hymenolepis diminuta. International Journal for Parasitology 13, 101–6.CrossRefGoogle ScholarPubMed
Seedmak, J. J. & Grossberg, S. E. (1977). A rapid, sensitive and versatile assay for protein using Coomassie Brilliant Blue G-250. Analytical Biochemistry 79, 544–52.CrossRefGoogle Scholar
Spies, J. R. (1957). Colorimetric procedures for amino acids. In Methods of Enzymology, vol. 3, (ed. Colowick, S. P. and Kaplan, N. O.), pp. 467–77. New York: Academic Press.Google Scholar
States, B. & Segal, S. (1969). Distribution of glutathione-cystine transhydrogenase activity in subcellular fractions of rat intestinal mucosa. Biochemical Journal 113, 443–4.CrossRefGoogle ScholarPubMed
Stekol, J. A. (1957). Preparation and determination of sulphur amino acids and related compounds. In Methods of Enzymology, vol 3, (ed. Colowick, S. P. and Kaplan, N. O.), pp. 578–600. New York: Academic Press.Google Scholar
Stipanuk, M. H. (1979). Effects of excess dietary methionine on the catabolism of cysteine in rats. Journal of Nutrition 102, 2126–39.CrossRefGoogle Scholar
Stipanuk, M. H. & Beck, P. W. (1982). Characterization of the enzymic capacity for cysteine desulphydration in liver and kidney of the rat. Biochemical Journal 206, 267–77.CrossRefGoogle ScholarPubMed
Stipanuk, M. H. & Benevenga, N. J. (1977). Effect of cystine on the metabolism of methionine in rats. Journal of Nutrition 107, 1455–67.CrossRefGoogle Scholar
Thong, K. -L. & Coombs, G. H. (1985). L-serine sulphydrase activity in trichomonads. IRCS Medical Science 13, 495–6.Google Scholar